Research workbench
AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A5FV66)
Analyse AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A5FV66) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5FV66
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6A9Ec001Bc00FA7B5ca9B36332E57e2641f2d127
- Molecule
- Phosphate acyltransferase
- UniProt
- A5FV66
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acyltransferase | protein | 380 | 47% helix, 15% strand | A5FV66 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 534 | 0.70 | 0.80 | 53 | empty |
| 2 | 123 | 0.41 | 0.75 | 17 | empty |
| 3 | 52 | 0.32 | 0.77 | 14 | empty |
| 4 | 76 | 0.31 | 0.74 | 21 | empty |
| 5 | 62 | 0.30 | 0.75 | 15 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5FV66
- Elsewhere: UniProt A5FV66 · AlphaFold DB A5FV66
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